INVESTIGADORES
PEICHOTO Maria Elisa
congresos y reuniones científicas
Título:
Purification and characterization of a cysteine rich secretory protein from Philodryas patagoniensis colubrid snake venom
Autor/es:
MARÍA ELISA PEICHOTO; PAMELA TEIBLER; STEPHEN P. MACKESSY; PAULA L. BURCKHARDT; MARÍA CRISTINA BRENO; OFELIA ACOSTA; MARCELO LARAMI SANTORO
Lugar:
San Pablo
Reunión:
Encuentro; X Annual Scientific Meeting of Butantan Institute; 2008
Institución organizadora:
Instituto Butantan
Resumen:
Introduction: Cysteine Rich Secretory Proteins (CRiSPs) are widespread in snake venoms. These proteins are suggested to be recruited into the venom protein repertoire very early in the evolution of snakes. However, the biological functions of most of them are still unknown. Objectives: In the present study, we aimed to purify and characterize a CRiSP from the venom of Philodryas patagoniensis (Pp-CRiSP), an opistoglyphous colubrid snake, frequently found in open areas of northeastern Argentina. Methods and Results: Purification of Pp-CRiSP was undertaken by chromatography on Mono-Q and Phenyl Sepharose, Pp-CRiSP was homogenous by SDS-PAGE, and it is a single-chain protein, with a molecular mass of 24,828 Da, whose amino-terminal sequence is homologous to other CRiSPs. The purified protein hydrolyzed neither azocasein nor fibrinogen, and it could not induce edema, hemorrhage nor inhibition of platelet adhesion and aggregation. In addition, Pp-CRiSP, up to a final concentration of 2 ìM, could not inhibit contractions of rat aortic smooth muscle induced by 60 mM KCl. However, Pp-CRiSP caused muscular damage to murine gastrocnemius muscle, an action that had not been previously described for snake venom CRiSPs. Discussion: Pp-CRiSP might play a key role in the pathogenesis of disturbances that occur during P. patagoniensis envenomation, especially due to its myotoxic activity. Moreover, this is the first report on the isolation and characterization of a CRiSP from the venom of a colubrid snake showing biological activity. Furthermore, Pp-CRiSP is the first CRiSP with toxic activity on skeletal muscle. Therefore, Pp-CRiSP will be important for studies of the structure-function and evolutionary relationships of this family of proteins widely distributed among snake venoms.